Sequences in both class II major histocompatibility complex α and β chains contribute to the binding of the superantigen toxic shock syndrome toxin 1

Ned S. Braunstein, Dominique A. Weber, Xiao Cun Wang, Eric O. Long, David Karp

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

Class II major histocompatibility complex (MHC) molecules present peptides derived from processed antigen to antigen-specific CD4-positive T cells. In addition, class II molecules bind with high affinity another class of antigens, termed superantigens. T cell stimulation by superantigens depends almost exclusively on the Vβ segment expressed by the T cell receptor (TCR). Mapping of the superantigen binding site on class II molecules should provide valuable information on how MHC and TCR molecules interact. Recombinant mouse I-A class II molecules expressed on transfected L cells were analyzed for their ability to bind the toxic shock syndrome toxin 1. Polymorphic residues in the α helices of both the α and β chains of I-A contributed to quantitative toxin binding, suggesting that the toxin binds to either a combinatorial or a conformational site on class II MHC molecules.

Original languageEnglish (US)
Pages (from-to)1301-1305
Number of pages5
JournalJournal of Experimental Medicine
Volume175
Issue number5
StatePublished - May 1 1992

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Superantigens
Major Histocompatibility Complex
T-Cell Antigen Receptor
T-Lymphocytes
Antigens
CD4 Antigens
Binding Sites
Peptides
Staphylococcal enterotoxin F

ASJC Scopus subject areas

  • Immunology

Cite this

Sequences in both class II major histocompatibility complex α and β chains contribute to the binding of the superantigen toxic shock syndrome toxin 1. / Braunstein, Ned S.; Weber, Dominique A.; Wang, Xiao Cun; Long, Eric O.; Karp, David.

In: Journal of Experimental Medicine, Vol. 175, No. 5, 01.05.1992, p. 1301-1305.

Research output: Contribution to journalArticle

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